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The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding studies reveal the location of the active site

Recent developments in NMR have extended the size range of proteins amenable to structural and functional characterization to include many larger proteins involved in important cellular processes. By applying a combination of residue-specific isotope labeling and protein deuteration strategies tailo...

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Hlavní autoři: Kelly, Mark J. S., Ball, Linda J., Krieger, Cornelia, Yu, Yihua, Fischer, Markus, Schiffmann, Susanne, Schmieder, Peter, Kühne, Ronald, Bermel, Wolfgang, Bacher, Adelbert, Richter, Gerald, Oschkinat, Hartmut
Médium: Artigo
Jazyk:Inglês
Vydáno: The National Academy of Sciences 2001
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On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC60818/
https://ncbi.nlm.nih.gov/pubmed/11687623
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.231323598
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